DB code: D00851
RLCP classification | 1.13.30000.10 : Hydrolysis | |
---|---|---|
CATH domain | 2.40.10.10 : Thrombin, subunit H | Catalytic domain |
2.40.10.10 : Thrombin, subunit H | Catalytic domain | |
E.C. | 3.4.21.19 | |
CSA | ||
M-CSA | ||
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
2.40.10.10 : Thrombin, subunit H | M00139 D00214 M00167 D00426 M00133 D00428 D00429 D00430 D00431 D00432 D00433 D00434 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00217 M00216 D00528 D00848 D00850 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | MEROPS | RefSeq |
---|---|---|---|---|
P0C1U8 |
Glutamyl endopeptidase
|
EC
3.4.21.19
Endoproteinase Glu-C Staphylococcal serine proteinase V8 protease V8 proteinase |
S01.269
(Serine)
|
|
Q99V45 |
Glutamyl endopeptidase
|
EC
3.4.21.19
Endoproteinase Glu-C Staphylococcal serine proteinase V8 protease V8 proteinase |
NP_371572.1
(Protein)
NC_002758.2 (DNA/RNA sequence) |
KEGG enzyme name |
---|
Glutamyl endopeptidase
V8 proteinase Endoproteinase Glu-C Staphylococcal serine proteinase |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P0C1U8 | SSPA_STAAU | Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa. | Secreted. | ||
Q99V45 | SSPA_STAAM | Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa. | Secreted (By similarity). |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | |||||||||
KEGG-id | C00017 | C00001 | C00017 | I00087 | I00085 | I00086 | |||||
E.C. | |||||||||||
Compound | Protein | H2O | Protein | Peptidyl-Ser-tetrahedral-intermediate (with previous peptide) | Acyl-enzyme(Peptidyl-Ser-acyl group) | Peptidyl-Ser-tetrahedral-intermediate | |||||
Type | peptide/protein | H2O | peptide/protein | ||||||||
ChEBI |
15377 15377 |
||||||||||
PubChem |
22247451 962 22247451 962 |
||||||||||
1wczA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1qy6A01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2o8lA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1wczA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1qy6A02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2o8lA02 | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Literature [4] & Swiss-prot;P0C1U8, Q99V45 |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1wczA01 | SER 169 | GLY 167;SER 169 | ||||||||
1qy6A01 | SER 169 | GLY 167;SER 169 | ||||||||
2o8lA01 | SER 169 | GLY 167;SER 169 | ||||||||
1wczA02 | HIS 51;ASP 93 | |||||||||
1qy6A02 | HIS 51;ASP 93 | |||||||||
2o8lA02 | HIS 51;ASP 93 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[3]
|
Figure 5, p.4505-4508 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 4509307 |
Journal | Proc Natl Acad Sci U S A |
Year | 1972 |
Volume | 69 |
Pages | 3506-9 |
Authors | Houmard J, Drapeau GR |
Title | Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 136253 |
Journal | Biochem Biophys Res Commun |
Year | 1976 |
Volume | 72 |
Pages | 411-7 |
Authors | Austen BM, Smith EL |
Title | Action of staphylococcal proteinase on peptides of varying chain length and composition. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12475199 |
Journal | Chem Rev |
Year | 2002 |
Volume | 102 |
Pages | 4501-24 |
Authors | Hedstrom L |
Title | Serine protease mechanism and specificity. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 69-342. |
Medline ID | |
PubMed ID | 14747701 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 2004 |
Volume | 60 |
Pages | 256-9 |
Authors | Prasad L, Leduc Y, Hayakawa K, Delbaere LT |
Title | The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus. |
Related PDB | 1qy6 2o8l |
Related UniProtKB | Q99V45 |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 17878159 |
Journal | J Biol Chem |
Year | 2007 |
Volume | 282 |
Pages | 34129-38 |
Authors | Nickerson NN, Prasad L, Jacob L, Delbaere LT, McGavin MJ |
Title | Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing. |
Related PDB | |
Related UniProtKB |
Comments |
---|
This enzyme belongs to peptidase family-S1B.
Since this enzyme has got the same catalytic site as trypsin, |
Created | Updated |
---|---|
2011-02-24 | 2012-07-31 |